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Results 1 - 10 of 10
EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.24Fe-4S-center midpoint potential value of + 340 mV. The midpoint potential value shifts slightly, to + 380 mV, in the N-ethylmaleimide-treated enzyme 702397
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.24Fe-4S-center presence of a unique iron site in the [4Fe-4S] cluster. Site-specific cluster chemistry, involving the formation of a five-coordinate Fe site with two cysteinate ligands, occurs during catalytic cycling of FTR 704156
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.24Fe-4S-center presence of a [Fe4S4]3+ cluster that is coordinated by five cysteinates with little unpaired spin density delocalized onto the cluster-associated cysteine of the active-site disulfide. While the ligation site of the fifth cysteine remains undefined, the best candidate is a cluster bridging sulfide 702198
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.24Fe-4S-center presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide 702192
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.24Fe-4S-center residues Cys52, Cys71, Cys73, and Cys82 bind the Fe-S cluster 703527
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.2FAD in each monomer, two conserved Rossmann-type modules form the FAD-binding. The pi-stacking interaction between the side chain of the conserved tryptophan at the C-terminal tail of a monomer and the isoalloxazine ring of the FAD of an adjacent monomer at its re-face. This interaction seems to protect the flavin from the solvent, a distinctive feature of the GvDTR enzyme not found in other flavin thioredoxin reductases. The C-terminal extension stabilizes the semiquinone state of the flavin 765599
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.2Ferredoxin - 741861, 741911, 743165, 743317, 743549, 743739, 765600, 765730
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.2Ferredoxin Fdx, iron-sulfur ferredoxin, enzyme-Fdx interaction analysis, overview. Investigation of GvDTR and GvFdx1 or GvFdx2 as functional redox partners by analyzing the reduction of photosynthetic m-type thioredoxin (Trxm) in a mixture containing NADPH, the redox pair Anabaena ferredoxin-NADP+ reductase (AnFNR)/GvFdx1 or AnFNR/GvFdx2, GvDTR, and Gloeobacter Trx-m (GvTrxm). The redox state of GvTrx-m is examined with the thiol-specific reagent 4-acetamido-40-maleimidyldistilbene-2,2'-disulfonic acid (AMS), separating the reduced and oxidized proteins with nonreducing SDS-PAG.Only GvFdx1 with the complete reactants significantly increases the reduced/oxidized ratio of GvTrx-m, prompting the conclusion that GvFFTR interacts with GvFdx1 but not with GvFdx2, which has a unique C-terminal extension. GvFdx1 is a functional electron-delivering partner for GvDTR. GvFdx1 binding to GvDTR is strictly dependent on the presence of the enzyme's C-terminal tail. GvFdx1 (petF, gvip492) and GvFdx2 (gvip440) are recombinantly expressed as N-terminally His8-tagged proteins, with a TEV cleavage site preceding the Fdx sequence, in Escherichia coli Rosetta (DE3) pLys cells 765599
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.2Ferredoxin ferredoxin-thioredoxin reductase forms an electrostatically stabilized 1:1 complex with ferredoxin. Chemical modification of three or four carboxyl groups on ferredoxin has little effect on its interaction with ferredoxin-thioredoxin reductase. The ferredoxin domain that binds ferredoxin-thioredoxin reductase is not completely identical to that involved in binding other ferredoxin-dependent enzymes 702476
Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.2[4Fe-4S]-center - 741861, 743549, 743739
Results 1 - 10 of 10